Ligand Triton X-100

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Basic Ligand Information

Molecular Structure
Picture of Triton X-100 (click for magnification)
Molecular Formula
BRENDA Name
InChIKey
C34H62O11
Triton X-100
IVKNZCBNXPYYKL-UHFFFAOYSA-N
Synonyms:
Triton, Triton-X-100, Triton-X100, Triton CF-54, Tritons, TritonX-100, Triton X100, Triton X 100

Roles as Enzyme Ligand

Substrate in Enzyme-catalyzed Reactions (5 results)

EC NUMBER
REACTION
REACTION DIAGRAM
LITERATURE
ENZYME 3D STRUCTURE
Triton X-100 + NAD+ = ? + NADH
show the reaction diagram
-

Activator in Enzyme-catalyzed Reactions (590 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
slight activation
-
120-190% activity at 0.1-0.5%
-
23% activation at 0.1%
-
activates
-
1%, 112% of initial activity
-
0.25% of TritonX-100 has slight improvement on enzyme activity, whereas 0.75% of TritonX-100 slightly inhibits the enzyme activity
-
addition to intact microsomes results in a concentration dependent increase in gulonolactone oxidase activity, 38% activation with 5 mg Triton X-100 per mg protein
-
5fold increase in activtiy of purified detergent-free enzyme
-
activates
-
solubilization with Triton X-100 gives 10fold increase in activity compared to solubilization with Tween 80, differential solubilization with Tween 80 + Triton X-100 gives 2fold higher activity than Triton X-100 alone
-
stimulates
-
activated by addition of 0.1% (v/v) Triton-X-100
-
5% w/v, 123% of initial activity
-
detergent required
-
activates by 7% at 1% w/v
-
0.1%, 3.7fold increase of specific activity of wild-tpye Gluc
-
stimulates activity by promoting the dissociation of inhibitory product from the enzyme
-
activation at 0.1% v/v
-
activation
-
700% activation at 0.025%
-
stimulates
-
0.01% (v/v) promotes small enhancement in activity
-
needs detergent, 0.04%
-
effect onto P-450 itself suggested
-
stimulates
-
effective inhibitor
-
at an optimal concentration of 0.1% Triton X-100, the detergent increases the rate of desaturation about three fold
-
stimulates
-
2% (v/v) Triton X-100 enhances the enzyme activity by 270%
-
106% activity at 1% (v/v)
-
leads to 50% stimulation at concentration of 0.01%
-
up to 17fold increase in methyl viologen dependent activity, loss of NADH dependent activity
-
concentration-dependent activation up to 2.8fold
-
0.01%, 25% increase in activity
-
stimulates, maximum value of ACO acitvity at 0.08%
-
restores activity during ischemia
-
1%, slight activation, effect not consistant
-
0.1-0.5%, increases activity about twofold
-
enzyme is inactive in absence of detergent or phospholipid. Triton X-100 gives optimal activity
-
increases activity
-
0-0.1% concentration, at most 30% activation
-
activating the enzyme membrane-bound in the microsomal fraction
-
0.5%, 10% activation
-
enhances activity, optimal concentration 0.04%
-
stimulation at 1%
-
0.1%, 4fold activation
-
0.1%, stimulates
-
activates at low concentrations by 50%
-
activation
-
i.e. octylphenoxy polyethoxyethanol, slight stimulation at 0.1 mg/ml
-
only CPTi
-
phospholipase activity for PagP depends on presence of Triton X-100, dodecylmaltoside, or Cyfos-7 in decreasing order of specific activity. Triton X-100 participates as a substrate in the palmitoyltransferase reaction
-
required for enzyme activity
-
1%, several fold activation, inhibition at 3%
-
leads to increasing turnover rate of acyl-CoA
-
25% activation at 0.1%
-
activation
-
activation
-
required for optimal activity, 0.01-0.015%
-
activation and stabilization, unstable without
-
strong requirement
-
optimum activity at 0.08-0.1%
-
maximum activation at 0.125%
-
stimulation, 0.1% v/v
-
stimulation, 0.1% v/v, inhibits at concentrations above 0.5% v/v
-
slight stimulation, 0.1% v/v
-
activation
-
detergent required
-
activation, 1.0-1.5%
-
between 0 and 0.5 mM Triton X-100 increases the apparent specific activity 5fold
-
enhances specificity and yield of beta-cyclodextrin production
-
0.1-0.5% slightly enhances activity
-
slightly stimulating
-
requirement, maximum activity at 0.5-2%
-
1 mM, 160% of initial activity
-
maximal activity at 133 critical micelle concentration or 32 mM or 2%, representing about 45% of that observed with dodecylmaltoside
-
maximal activity in a detergent mixture, Triton X-100/Cutscum (1:2, v/v), 0.1 mg/ml
-
maximum activity at 0.05%. Inhibitory above 0.2%; maximum activity at 0.5%, inhibitory above 2%
-
0.8%, activation
-
0.1-5%, 1.5fold stimulation
-
0.1%, 2fold stimulation
-
activates
-
at room temperature 2fold increase in reation rate, in excess inhibitory
-
stimulates solubilized activity
-
1.7fold at 0.04%
-
1.4fold activation at 5% (w/v)
-
activity increases as the Triton X-100 concentration is increased from 0 to 0.2%. Higher concentrations of detergent are inhibitory
-
high activation at 0.5%
-
0.1%, stimulates enzyme of isolated plasma membrane
-
enhances activity
-
transferase—transfer of the 4-amino-4-deoxy-alpha-L-arabinose unit from its putative isoprenoid carrier, undecaprenyl phosphate-4-amino-4-deoxy-alpha-L-arabinose, to the radiolabeled acceptor [4'-32P]lipid IV(A) is dependent upon the presence of the nonionic detergent Triton X-100, with maximal activity observed at 0.2% in the assay system
-
stimulates activity
-
stimulates activity
-
stimulates activity of enzyme form A. Enzyme form B is fully active in absence of detergents. Detergents stimulate the activity of enzyme form A by lowering the KD and KM of CMP-N-acetylneuraminate and increasing the Vmax of the reaction
-
the enzymatic activity is dependent upon the presence of Triton X-100. At concentrations greater than 0.1% Triton X-100, the transferase activity is inhibited
-
0.1 w/v, 5fold stimulation
-
0.025%, activates 1.5times
-
required for enzymatic activity, optimal concentration: 0.01%
-
approximately increases the activity of the enzyme 2fold and retains the effect at a similar level through various concentrations from 0.01 to 1%
-
detergent stimulates activity, maximally active in presence of 0.1% Triton X-100
-
not strictly dependent on TRiton X-100, maximum activity at 0.01% Triton X-100
-
activates
-
activates
-
Antagonizing the effect of all inhibitors identified with GgIP3K-A. When 0.2% Triton X-100 is added to assays containing the respective inhibitors at IC50, the previous inhibition of GgIP3K-A is immediately reversed by an extent between 49 and 100%
-
0.01%, increases activity
-
50% increase of activity of the bound enzyme only
-
required
-
the detergent increases Cdk5-p35 activity with histone H1 and the autophosphorylation at p35
-
DNA polymerase is stabilized with an approximately 25% increase in enzyme activity
-
or CHAPS, absolutely required
-
activation, only membrane-bound Golgi-enzyme
-
slightly stimulates with Mn2+, but not with Mg2+ as cofactor
-
stimulates at low subsolubilizing concentrations, membrane-solubilizing concentrations lead to nearly complete inactivation
-
optimal activation at 0.2%, w/v
-
optimal concentration is 50-120 mM
-
activity is dependent on TRiton X-100
-
0.5%, stimulates
-
maximal activity is obtained with a Triton X-100:phospholipid ratio of 1:1
-
maximal activation at 0.015%
-
0.4% Triton X-100 is optimal for enzyme activity
-
strongly activating, best at 0.3% w/v. Absence of this detergent causes the inactivation of ckGL even in the enzyme assay, as it does during the purification
-
stimulates
-
stimulation
-
1% elevates Vmax without affecting Km
-
5%, 190% of initial activity
-
at 0.001% (w/v) 120% activity
-
stimulation
-
slight activation at 10 mM
-
about 60% stimulation, optimum activity at 0.02%
-
presence of 0.01% Triton X-100 enhances isoform SerB2 activity by 15-20%
-
0.1%, 25-30% activation
-
addition of Triton X-100 stimulates DGPP phosphatase activity to a maximum at a concentration of 2 mM
-
; 210.5% of initial isozyme Nuc1 activity at 1%
-
biphasic, optimal stimulation at 1 mM
-
increase of enzyme activity
-
activation, best at 1-2 mM
-
maximally active at 0.05%, higher concentrations reduce activity. Synergistic activation of the enzyme by spermine and CaCl2 or by spermine and Triton X-100 is not observed
-
activates
-
0.3% activates
-
0.05 g/l, stimulates
-
requirement, membrane-bound enzyme
-
about 105% activity at 1 mM
-
110% activity at 1 mM
-
isoform Ag-I shows 110% activity at 1% (v/v) Triton X-100
-
0.01%, enhances activity
-
10 mM, 138% of initial activity activity
-
0.1%, 162% increase in activity
-
1%, 1.9fold activation
-
10-20% stimulation
-
prevents loss of activity caused by dilution
-
about 115% activity at 1% (v/v)
-
reagent in the preincubation mixture at concentrations 0.05-1% activates the enzyme by 45-72%
-
activates the wild-type enzyme by 33% at 0.1% v/v
-
maximal stimulation at 0.03%, or small amounts of other detergents
-
30 mg/ml, 1.2fold activation
-
106.7% activity at 1% (v/v)
-
stimulates
-
0.01%
-
0.01%, 123% of initial activity
-
0.1%, activates
-
required for maximal activity
-
208.82% relative activity at 0.05% (v/v)
-
slight increases (over 10%)
-
218.51% relative activity at 0.05% (v/v)
-
310.29% relative activity at 0.01% (v/v)
-
stimulates the catalytic efficiency of serotype A 35fold
-
optimally activating at 0.140 mM, at concentrations above the critical micelle concentration
-
161.26% activity at 1% (v/v)
-
increases activity of the enzyme
-
membrane-associated form
-
optimum concentration: 0.05%
-
activation, 180% activity
-
enzyme solubilized, activation
-
slight activation, activation depending on increasing concentrations of Triton X-100
-
activates
-
0.1% Triton X-100: 6-10fold activation
-
optimum activity above 0.14%, stable up to 4.2%
-
6fold increase at 0.5%
-
stimulation in hydrolysis as the detergent concentration approaches the critical micelle concentration of 0.19 mM
-
about 115% activity at 5 mM
-
0.03-0.05% (v/v)
-
highest conversion yield at a 0.75% without affecting the diastereoselectivity ratio
-
at 0.04% 30fold higher activity than at 1%
-
Trion X-100 leads to the emergence of the highest relative activity at 0.02% (v/v)
-
slightly activating at 0.001%, slightly inhibitory at 0.01%
-
stimulates
-
activation, above critical micelle concentration, inhibition from 0.05% to 0.5%
-
activation
-
5 mM, 4.6fold activation
-
at 0.05% highest activity of the enzyme
-
the enzyme requires Triton X-100 or deoxycholate for maximal activity
-
stimulates
-
activation
-
stimulates
-

Inhibitor in Enzyme-catalyzed Reactions (458 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
10% (w/v), 78% inhibition
-
1% v/v, 88% residual activity
-
immediate loss of 60-70% activity, remaining activity is stable for 4 days, competitive vs. testosterone, non-competitive vs. NAD+
-
potent inhibition at 0.01-0.1%
-
0.006 mM, 50% inhibition of chloroplastic form and 52% inhibition of cytosolic form
-
1% w/v, 67% residual activity
-
0.25% of TritonX-100 has slight improvement on enzyme activity, whereas 0.75% of TritonX-100 slightly inhibits the enzyme activity
-
1 mM, 35% inhibition
-
0.5%, inactivation
-
0.5%, complete inhibition
-
0.1%, no residual activity
-
about 50% residual activity at 2% (v/v)
-
concentration higher than 0.5% deactivates the enzyme
-
at 1% w/v by over 50%
-
strong reversible inhibition
-
dose-dependent inhibition
-
1% (v/v) promotes inhibition of activity
-
6% loss of activity at 0.1% detergent and 59% loss of activity at 0.3% detergent
-
13% residual activity at 0.25 mM
-
33-66% residual activity at 5 and 10% (v/v)
-
VKOR activity is dramatically decreased in Triton X-100
-
inhibits reduction of plastoquinone
-
inactivation at high concentrations
-
at a final concentration of 0.01%
-
inhibitory at above 0.5%
-
inhibits at concentration of 0.5%
-
complete loss of NADH dependent activity at concentration of 0.05%, up to 17fold increase in methyl viologen dependent activity
-
irreversible inactivation
-
no activity at 2 mg/ml
-
1% w/v, 84% residual activity
-
1.0%, 15% inhibition
-
inhibitory for the solubilized enzyme
-
; 1%, complete inhibition
-
0.1%, 63% inhibition
-
inactivation, reversible by addition of lipids: cardiolipin, phosphatidylglycerol, and especially phosphatidylserine
-
no activity when used to solubilize enzyme
-
inhibition reversed by albumin
-
75 and 95% inhibition at 0.2 and 0.6 mM respectively due to detergent
-
high concentration, stimulation at low concentration
-
activation at 0.1% v/v, inhibition at higher concentrations, pig stomach
-
weak inhibition
-
strong
-
at concentrations above 0.5%
-
as the concentration of Triton X-100 increases from 0 to 0.5% in the reaction mixture, the activity of the enzyme decreases but is maintained at about 60% of the original activity, up to 6% Triton X-100
-
0.25-1%
-
at high concentrations
-
in excess, phospholipids protect
-
at 0.1% and 0.2% concentrations has no effect, at a concentration of 1%, there is a 47% inhibition of enzyme activity
-
activity increases as the Triton X-100 concentration is increased from 0 to 0.2%. Higher concentrations of detergent are inhibitory
-
detergent solubilization of cell membranes specifically abolishes ADP-ribosylation of high MW histones
-
above critical micelle concentration of 0.016%, 15% inhibition, reversible
-
at higher concentrations
-
the enzymatic activity is dependent upon the presence of Triton X-100. At concentrations greater than 0.1% Triton X-100, the transferase activity is inhibited
-
above 0.2%
-
stimulates farnesyl-transferring activity, inhibits dimethylallyl-transferring activity
-
0.2%, total inhibition
-
0.05%, 53% inhibition
-
above 0.5% w/v, activation below
-
0.5%, almost complete inhibition
-
inhibition kinetics, overview. No inhibition by monoacylglycerol
-
IC50: 0.054 mM
-
0.1%, 96% inhibition
-
activity is lost upon addition, can be restored by addition of lipid fractions to the assay
-
substrate protects from inhibition
-
inhibitory at higher concentrations
-
0.2 mM, 50% inhibition. Concentrations higher than 0.6 mM result in an almost complete inhibition
-
inhibits activity as the molar ratio of Triton X-100 to CDP-diacylglycerol raises beyond the point of maximal activity
-
0.5%, about 95% inhibition
-
slight
-
inhibits about 50% at 0.25%
-
67.3% residual activity at 0.05% (v/v)
-
10% inhibition at 0.25%
-
uncompetitive inhibition at 0.01%, below the critical micelle concentration, and above at concentration higher than 0.013%
-
35% inhibition at 1 mM; 55% inhibition at 1 mM
-
above 0.1%
-
10 mM, 20-30% inhibition
-
strong inhibition of 4-nitrophenylacetate hydrolysis
-
inhibits isoenzyme AP-1
-
20% of activity remaining with 1%
-
0.2% causes 100% inhibition
-
inhibits PLC-beta1 activity
-
about 30% residual activity at 0.1% (v/v)
-
0.3 mM, 64% inhibition
-
1 mM, 15% residual activity, free enzyme, 35% residual activity, immobilized enzyme, respectively
-
11% residual activity in the presence of 5% (v/v) Tween 80, after 60 min at 70°C
-
1% v/v, 72% of initial activtiy
-
88% residual activity at 1 mM
-
61% residual activity at 10% (v/v)
-
moderately inhibits enzyme activity by 3%-30% at different concentrations
-
strongly inhibits the activity even at a low concentration
-
96.6% residual activity at 0.1% (v/v)
-
98.6% residual activity at 0.5% (w/v)
-
slightly effective
-
5 mM, about 40% loss of activity
-
inhibits at 0.1-0.5%
-
1 mg/ml, 4% inhibition
-
5 mM, 71% residual activity
-
0.05%
-
complete inactivation at 0.05%
-
at 37°C and pH of 7.5, 0.01% reduces prosubtilisin JB1 relative activity to 92% and 0.05% reduces prosubtilisin JB1 relative activity to 69%
-
30-80% loss of activity, thiobenzyl benzyloxycarbonyl-L-lysinate as substrate
-
non-specific inhibition in the presence of 0.02% (v/v) Triton X-100
-
0.2%, 60% residual activity
-
slight inhibition at 50 mM
-
87% residual activity at 0.01% (v/v)
-
37% inhibition at 1%
-
significantly decreases enzyme binding to elastin
-
optimally activating at 0.140 mM, at concentrations above the critical micelle concentration
-
0.1%, 24% inhibition
-
40% inhibition at 1%
-
5 mg/ml: 42% inhibition
-
activates the hydrolytic reaction, best at 0.5% w/v, but inhibits the synthetic reaction
-
0.01%
-
35% inhibition at 1%, 83% at 5%
-
50% inhibition
-
inhibitory effect in decreasing order: EDTA, SDS, Triton X-100, Tween 20
-
1% (w/v): 12% of maximal activity
-
strong inactivator
-
0.1%, 64% residual activity
-
weak inhibition
-
slightly activating at 0.001%, slightly inhibitory at 0.01%
-
1 mM, 83% of initial activity
-
increases activity of nuclear membrane enzyme, activity of nuclear sap and chromatin non-histone enzyme untouched or decreased
-
0.05-0.5%, activation at 0.02%
-
30% inhibition at 0.1%, 20% at 1%
-
0.5%
-
96% inhibition
-
strong inhibition
-
specific inhibition
-
uncompetitive inhibition of verapamil-induced Pgp ATPase activity
-

Metals and Ions (10 results)

EC NUMBER
COMMENTARY
LITERATURE
ENZYME 3D STRUCTURE
activates slightly
-
2.2 mM, activates the wild-type and mutant enzymes, poxB3 and poxB4, 32-, 4-, and 6fold, respectively. With the addition of alpha-chymotrypsin the activation of the mutant enzymes poxB3 and poxB4 is increased 14- and 39fold, respectively
-
3 Triton (T1, T2, and T3) are located in the two monomers with one on the top portion of the active site tunnel in monomer A and the other two occupying the overall tunnel of monomer B
0.1% v/v, 1.3fold activation. 1% v/v, 31% loss of activity
-
activates at 0.5%
-
110% activity at 1% (v/v)
-
about 20% activation
-
0.5%, 123% of initial activity
-
the enzyme activity is significantly promoted at 1 mM Triton X-100
-
activates slightly at 0.5-1 mM
-

3D Structure of Enzyme-Ligand-Complex (PDB) (3 results)

EC NUMBER
ENZYME 3D STRUCTURE

Enzyme Kinetic Parameters

Ki Value (7 results)

EC NUMBER
KI VALUE [MM]
KI VALUE MAXIMUM [MM]
COMMENTARY
LITERATURE
0.09
-
-

IC50 Value (2 results)

EC NUMBER
IC50 VALUE
IC50 VALUE MAXIMUM
COMMENTARY
LITERATURE
0.054
-
IC50: 0.054 mM
1.3
-
pH 7.5, 25°C

References & Links